Module 5

Question 1

Describe the basics of protein structure

Answer 1

Question 2

Describe enzymes

Answer 2

Question 3

how can you measure reaction rate (velocity)

Answer 3

Question 4

What is initial velocity

Answer 4

Vo is used to get non-attenuated rates
-Ideally measured quickly and for a short period of time (before 10% of substrate is used up)
-Vo = -Change [S]/ change in time
-Overall reaction speed = time 1 + time 2
-Under optimal conditions and excess substrate, the limiting step is the catalytic step

Question 5

Explain the michaelis-menten equation

Answer 5

Question 6

Describe the difference in Km values of hexokinase and glucokinase

Answer 6

Hexokinase:
-Low Km, works fast even if little substrate is present

Glucokinase:
-High Km, works fast only when theres a lot of substrate present
-ATP signals to glucose sensor

Question 7

Explain ALDH1 and ALDH2 in ‘alcohol allergy’

Answer 7

Question 8

What is the function of the Lineweaver-burk plot

Answer 8

Question 9

How does the Lineweaver-burk plot visualize the mechanism of inhibition

Answer 9

Question 10

What is competitive inhibition

Answer 10

Question 11

Describe methanol and competitive inhibition

Answer 11

Question 12

What is uncompetitive inhibition

Answer 12

Question 13

Describe uncompetitive inhibition of HIV reverse transcriptase

Answer 13

Question 14

What is noncompetitive inhibition

Answer 14

may be more selective

Question 15

how can you quantify and measure enzyme activity and specific activity?

Answer 15

-Increase in specific activity indicates purification of enzyme
-Activity is just a concentration
-1U/mg is highest specific activity attainable